Proteases (Serine)
The large family of serine proteases (almost one-third of all proteases; EC 3.4.21.-) is characterized by its general mechanism of action to cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the (enzyme's) active site. The members of this family can be divided roughly into four sub-groups based on their structure, being chymotrypsin-like (trypsin-like), subtilisin-like, carboxypeptidase Y-like, and Clp-like[1].
[1] L. Hedstrom. Serine Protease Mechanism and Specificity. Chem. Rev. 2002, 102, 4501-4524.
| Axon ID | Name | Description | From price | |
|---|---|---|---|---|
| 2734 | TM 5441 | Orally active inhibitor of PAI-1 | €105.00 | |
| 2344 | TM 5275 | Selective and orally active inhibitor of PAI-1 | €105.00 | |
| 1383 | Tiplaxtinin | Plasminogen activator inhibitor-1 (PAI-1) inhibitor | €70.00 | |
| 1769 | T 1776Na | Inhibitor of plasminogen activator inhibitor-1 | €80.00 | |
| 2838 | SK-216 | Specific inhibitor of PAI-1 | €105.00 | |
| 3710 | PAZ-417 | Potent, orally active and CNS-penetrant PAI-1 inhibitor | €130.00 | |
| 3294 | HSP47 inhibitor III | Inhibitor of the collagen-specific chaperone HSP47 | €120.00 | |
| 3568 | Col003 | Potent, competitive collagen-Hsp47 interaction inhibitor | €110.00 | |
| 3590 | ACT001 | PAI-1 inhibitor | €210.00 | |